CCA1_SCHPO
ID CCA1_SCHPO Reviewed; 500 AA.
AC Q9UTQ0;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 2.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=tRNA nucleotidyltransferase cca1 {ECO:0000303|PubMed:30528393};
DE EC=2.7.7.- {ECO:0000269|PubMed:30528393};
DE AltName: Full=CC-adding enzyme cca1 {ECO:0000303|PubMed:30528393};
DE AltName: Full=tRNA cytidyltransferase cca1 {ECO:0000303|PubMed:30528393};
GN Name=cca1 {ECO:0000303|PubMed:30528393}; ORFNames=SPAC1093.04c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION, DOMAIN, CATALYTIC ACTIVITY, AND MUTAGENESIS OF HIS-121.
RX PubMed=30528393; DOI=10.1016/j.bbrc.2018.11.131;
RA Reid N.E., Ngou J.S., Joyce P.B.M.;
RT "Schizosaccharomyces pombe contains separate CC- and A-adding tRNA
RT nucleotidyltransferases.";
RL Biochem. Biophys. Res. Commun. 508:785-790(2019).
RN [3]
RP FUNCTION.
RX PubMed=30988468; DOI=10.1038/s41592-019-0370-6;
RA Preston M.A., Porter D.F., Chen F., Buter N., Lapointe C.P., Keles S.,
RA Kimble J., Wickens M.;
RT "Unbiased screen of RNA tailing activities reveals a poly(UG) polymerase.";
RL Nat. Methods 16:437-445(2019).
CC -!- FUNCTION: tRNA nucleotidyltransferase involved in the synthesis of the
CC tRNA CCA terminus. In contrast to what is usually observed in
CC eukaryotes for which one enzyme synthesizes the whole tRNA CCA
CC terminus, in S.pombe, cca1 specifically adds two cytidine residues to a
CC tRNA substrate lacking this sequence while cca2 specifically adds the
CC terminal adenosine residue thereby completing the CCA sequence.
CC {ECO:0000269|PubMed:30528393, ECO:0000269|PubMed:30988468}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a tRNA precursor + 2 CTP = a tRNA with a 3' CC end + 2
CC diphosphate; Xref=Rhea:RHEA:60008, Rhea:RHEA-COMP:10465, Rhea:RHEA-
CC COMP:15488, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:74896,
CC ChEBI:CHEBI:83069; Evidence={ECO:0000269|PubMed:30988468};
CC -!- DOMAIN: Cca1 contains two alpha-helices (His-81 to Thr-86 and Glu-479
CC to Asp-484) and a beta-sheet (His-120 to Lys-131) that are not seen in
CC cca2, suggesting that cca1 has lost A-adding activity because this
CC beta-sheet reduces the flexibility of the loop (Asp-122 to Glu-139) as
CC compared to CCA- and A-adding enzymes. {ECO:0000305|PubMed:30528393}.
CC -!- DOMAIN: The ERhxxExxxhh motif (residues 231-241) has been suggested to
CC serve to distinguish between A-adding and CC-adding proteins as A-
CC adding enzymes have a small amino acid in the first position while CC-
CC adding enzymes have an E in the first position.
CC {ECO:0000305|PubMed:30528393}.
CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC polymerase family. {ECO:0000305}.
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DR EMBL; CU329670; CAB60249.2; -; Genomic_DNA.
DR PIR; T50067; T50067.
DR RefSeq; NP_594651.2; NM_001020080.3.
DR AlphaFoldDB; Q9UTQ0; -.
DR BioGRID; 279415; 2.
DR STRING; 4896.SPAC1093.04c.1; -.
DR SwissPalm; Q9UTQ0; -.
DR MaxQB; Q9UTQ0; -.
DR PaxDb; Q9UTQ0; -.
DR EnsemblFungi; SPAC1093.04c.1; SPAC1093.04c.1:pep; SPAC1093.04c.
DR GeneID; 2542977; -.
DR KEGG; spo:SPAC1093.04c; -.
DR PomBase; SPAC1093.04c; cca1.
DR VEuPathDB; FungiDB:SPAC1093.04c; -.
DR eggNOG; KOG2159; Eukaryota.
DR HOGENOM; CLU_019592_2_1_1; -.
DR InParanoid; Q9UTQ0; -.
DR OMA; CVSHIEV; -.
DR PhylomeDB; Q9UTQ0; -.
DR PRO; PR:Q9UTQ0; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; EXP:PomBase.
DR GO; GO:0005739; C:mitochondrion; EXP:PomBase.
DR GO; GO:0002135; F:CTP binding; IDA:PomBase.
DR GO; GO:0052928; F:CTP:3'-cytidine-tRNA cytidylyltransferase activity; IDA:PomBase.
DR GO; GO:0052927; F:CTP:tRNA cytidylyltransferase activity; IDA:PomBase.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IDA:PomBase.
DR GO; GO:0001680; P:tRNA 3'-terminal CCA addition; IDA:PomBase.
DR CDD; cd05398; NT_ClassII-CCAase; 1.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002646; PolA_pol_head_dom.
DR InterPro; IPR032828; PolyA_RNA-bd.
DR Pfam; PF01743; PolyA_pol; 1.
DR Pfam; PF12627; PolyA_pol_RNAbd; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
PE 1: Evidence at protein level;
KW Nucleotidyltransferase; Reference proteome; RNA-binding; Transferase;
KW tRNA-binding.
FT CHAIN 1..500
FT /note="tRNA nucleotidyltransferase cca1"
FT /id="PRO_0000139089"
FT REGION 122..139
FT /note="Flexible loop"
FT /evidence="ECO:0000305|PubMed:30528393"
FT MOTIF 231..241
FT /note="ERhxxExxxhh motif"
FT /evidence="ECO:0000305|PubMed:30528393"
FT MUTAGEN 121
FT /note="H->E: Restores the B/A element but does not restore
FT A-adding activity."
FT /evidence="ECO:0000269|PubMed:30528393"
SQ SEQUENCE 500 AA; 57553 MW; 6E9BC1B74F457BFE CRC64;
MASSSSILEL NETEKELSDI FLNVSKKIGQ MDRKEPEVRF AGGWVRDKLL RIESHDIDVA
IDCMSGFEFA QHLQSYLAQQ HPDWETKVIK IDANPLKSKH LETATARIMG MDIDIVNLRH
HDYTNSNSSN KLVFGTPLED ALRRDATINA LFYNLKSKTV EDFTGKGLVD LSNKIIRTPL
VADETFGDDP LRAVRCIRFA TKYDFNIHEE TIKGLKNPEL HERLRSSISR ERIGVEVDKM
LKHCNTNRAL KIIHSLGMFA CIFGPLEIHT KKLQSKNIES LSLIPYAIDL FGYLQKKDVS
IKNLSSSSKY IFWLAIATLP WYNWSILEKS KIKILPPILI RDSLKYSKPI MSQVENFFVH
YPLIMSKINV LEKEGKLTRL GCGRLVRELG PHWRDIIDWA FFMNTLISNS DIQRLNKDEE
VTWFHVLVKH IEEYGMEEAY NIQPIINGNE ITRILGIRPG PHLRKMLDDS IEWRIQNPES
TKEDYIAIML EKGTSAVVDS
